Analysis of the molecular species of the chick oviduct progesterone receptor using isoelectric focusing

P A Boyd, T C Spelsberg


Conditions are described for the preparative isoelectric focusing in flat beds of Sephadex of the progesterone receptor from the chick oviduct. The method allows the fractionation of the receptor into two molecular species, one focusing at pI 6 and the other at pI 7 with good purification and recovery. The pI 6 and pI 7 receptor species were purified 2- and 26-fold, respectively. The assaying of the focused fractions with the charcoal binding method provides an accurate identification and quantitation of the [3H]progesterone receptor. The method is reproducible in recovery, quantitation, and resolution of the two receptor species. The receptor with an apparent pI of 6 sediments at approximately 4 S on linear sucrose gradients, while the receptor with an apparent pI of 7 sediments at approximately 3.5 S. On the basis of the sedimentation values and elution patterns from diethylaminoethyl (DEAE) chromatography, the pI 6 component is equivalent to the "B" receptor species and the pI 7 component is equivalent to the "A" receptor species described previously [schrader, W, T., 7 O'Malley, B. W. )1972) J. Biol. Chem. 241, 51--59].


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Jul 4, 2006·Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology·Ignacio Camacho-ArroyoGenoveva González-Morán
Aug 15, 1986·Archives of Biochemistry and Biophysics·B O FangerJ A Cidlowski
Feb 24, 1997·Biochemical and Biophysical Research Communications·H SyväläP Tuohimaa


Jan 1, 1979·Journal of Steroid Biochemistry·W A CotyB W O'Malley
Jun 15, 1973·Annals of the New York Academy of Sciences·B J Radola
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Related Concepts

Animal Oviduct
Progesterone, (9 beta,10 alpha)-Isomer
Fallopian Tubes
Purification Aspects
Sedimentation Procedure
Chemical Fractionation
Receptors, Progesterone
Isoelectric Focusing

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